OSB2_ARATH
ID OSB2_ARATH Reviewed; 371 AA.
AC Q8GXH3; O49428; Q2V3G8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Protein OSB2, chloroplastic;
DE AltName: Full=Organellar single-stranded DNA-binding protein 2;
DE AltName: Full=Protein FLORAL ABSCISSION ASSOCIATED;
DE AltName: Full=Protein PLASTID TRANSCRIPTIONALLY ACTIVE 9;
DE Flags: Precursor;
GN Name=OSB2; Synonyms=FAA, PTAC9; OrderedLocusNames=At4g20010;
GN ORFNames=F18F4.110;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION.
RX PubMed=16326926; DOI=10.1105/tpc.105.036392;
RA Pfalz J., Liere K., Kandlbinder A., Dietz K.-J., Oelmueller R.;
RT "pTAC2, -6, and -12 are components of the transcriptionally active plastid
RT chromosome that are required for plastid gene expression.";
RL Plant Cell 18:176-197(2006).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=16990374; DOI=10.1093/jxb/erl130;
RA Butenko M.A., Stenvik G.-E., Alm V., Saether B., Patterson S.E.,
RA Aalen R.B.;
RT "Ethylene-dependent and -independent pathways controlling floral abscission
RT are revealed to converge using promoter::reporter gene constructs in the
RT ida abscission mutant.";
RL J. Exp. Bot. 57:3627-3637(2006).
RN [7]
RP FUNCTION, DNA-BINDING, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=17189341; DOI=10.1105/tpc.106.042028;
RA Zaegel V., Guermann B., Le Ret M., Andres C., Meyer D., Erhardt M.,
RA Canaday J., Gualberto J.M., Imbault P.;
RT "The plant-specific ssDNA binding protein OSB1 is involved in the
RT stoichiometric transmission of mitochondrial DNA in Arabidopsis.";
RL Plant Cell 18:3548-3563(2006).
CC -!- FUNCTION: Binds preferentially single-stranded DNA. Does not bind to
CC RNA. {ECO:0000269|PubMed:17189341}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:17189341}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8GXH3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8GXH3-2; Sequence=VSP_038020;
CC -!- TISSUE SPECIFICITY: Expressed in the floral abscission zone.
CC {ECO:0000269|PubMed:16990374}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:17189341}.
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DR EMBL; AL021637; CAA16609.1; -; Genomic_DNA.
DR EMBL; AL161552; CAB79001.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84260.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84261.1; -; Genomic_DNA.
DR EMBL; AK118242; BAC42861.1; -; mRNA.
DR EMBL; BT026461; ABH04568.1; -; mRNA.
DR PIR; T04885; T04885.
DR RefSeq; NP_001031674.1; NM_001036597.2. [Q8GXH3-2]
DR RefSeq; NP_567593.1; NM_118120.5. [Q8GXH3-1]
DR AlphaFoldDB; Q8GXH3; -.
DR SMR; Q8GXH3; -.
DR STRING; 3702.AT4G20010.1; -.
DR PaxDb; Q8GXH3; -.
DR PRIDE; Q8GXH3; -.
DR ProteomicsDB; 248828; -. [Q8GXH3-1]
DR EnsemblPlants; AT4G20010.1; AT4G20010.1; AT4G20010. [Q8GXH3-1]
DR EnsemblPlants; AT4G20010.2; AT4G20010.2; AT4G20010. [Q8GXH3-2]
DR GeneID; 827746; -.
DR Gramene; AT4G20010.1; AT4G20010.1; AT4G20010. [Q8GXH3-1]
DR Gramene; AT4G20010.2; AT4G20010.2; AT4G20010. [Q8GXH3-2]
DR KEGG; ath:AT4G20010; -.
DR Araport; AT4G20010; -.
DR TAIR; locus:2119767; AT4G20010.
DR eggNOG; ENOG502QPSC; Eukaryota.
DR HOGENOM; CLU_035942_0_0_1; -.
DR InParanoid; Q8GXH3; -.
DR OMA; QNPAKWW; -.
DR OrthoDB; 1476527at2759; -.
DR PhylomeDB; Q8GXH3; -.
DR PRO; PR:Q8GXH3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8GXH3; baseline and differential.
DR Genevisible; Q8GXH3; AT.
DR GO; GO:0042644; C:chloroplast nucleoid; HDA:TAIR.
DR GO; GO:0042645; C:mitochondrial nucleoid; IBA:GO_Central.
DR GO; GO:0009295; C:nucleoid; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:TAIR.
DR GO; GO:0006264; P:mitochondrial DNA replication; IBA:GO_Central.
DR GO; GO:0051096; P:positive regulation of helicase activity; IBA:GO_Central.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR000424; Primosome_PriB/ssb.
DR InterPro; IPR011344; ssDNA-bd.
DR PANTHER; PTHR10302; PTHR10302; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR PROSITE; PS50935; SSB; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; DNA-binding; Plastid;
KW Reference proteome; Repeat; Transit peptide.
FT TRANSIT 1..20
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 21..371
FT /note="Protein OSB2, chloroplastic"
FT /id="PRO_0000383609"
FT DOMAIN 97..195
FT /note="SSB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00252"
FT REGION 45..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..289
FT /note="PDF region 1"
FT REGION 312..360
FT /note="PDF region 2"
FT VAR_SEQ 222..223
FT /note="AR -> GI (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_038020"
FT CONFLICT 97
FT /note="V -> A (in Ref. 3; BAC42861)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 371 AA; 41729 MW; 115374D9ED7622AA CRC64;
MSLISKSLAR IECSPFFYPR ASEITTGKRI TSPQIRLYTA AAVGGKTGNG ERKQRAKAPA
KTPEAVTPVK PLEIASVTAT TENELPRPNE IAYESEVANW VNLIGFVDQP VQFEASSDGK
FWAGTVISQR SASDSSGFWI PIIFEGDLAK TAARYVSKDD QIHVSGKLFI DSPPPNMTYA
QANVQVLVQN LNFIQPMSPS PSPFMVMSSS EKEESGIKKQ PARAKQDIVI DEASDSWNHL
IENPKEWWDH RENKVNGLVK PRHPDFKSKD SSFSLWLNKA PNWVLPKLEG LEFDVLVPKA
RVVKQLKGEE SWKDLVQNPD KWWDNRIDKR NAKAPDFKHK ETGEALWLNE SPTWVLPKLP
PVKKKQESIV F
